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P15651 (ACADS_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Short-chain specific acyl-CoA dehydrogenase, mitochondrial

Short name=SCAD
EC=1.3.8.1
Alternative name(s):
Butyryl-CoA dehydrogenase
Gene names
Name:Acads
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length412 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Butanoyl-CoA + electron-transfer flavoprotein = 2-butenoyl-CoA + reduced electron-transfer flavoprotein.

Cofactor

FAD.

Pathway

Lipid metabolism; mitochondrial fatty acid beta-oxidation.

Subunit structure

Homotetramer. Ref.2

Subcellular location

Mitochondrion matrix.

Miscellaneous

A number of straight-chain acyl-CoA dehydrogenases of different substrate specificities are present in mammalian tissues.

Sequence similarities

Belongs to the acyl-CoA dehydrogenase family.

Sequence caution

The sequence AAA40669.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbutyrate catabolic process

Inferred from direct assay PubMed 3968063. Source: RGD

fatty acid beta-oxidation

Traceable author statement Ref.2. Source: RGD

fatty acid beta-oxidation using acyl-CoA dehydrogenase

Inferred from direct assay PubMed 3968063. Source: RGD

protein homotetramerization

Inferred from direct assay PubMed 3968063. Source: RGD

response to glucocorticoid

Inferred from expression pattern PubMed 8226958. Source: RGD

response to starvation

Inferred from expression pattern PubMed 8226958. Source: RGD

   Cellular_componentmitochondrial matrix

Inferred from direct assay PubMed 3813556. Source: BHF-UCL

mitochondrial membrane

Inferred from direct assay PubMed 3813556. Source: BHF-UCL

mitochondrion

Inferred from direct assay PubMed 3968063. Source: RGD

   Molecular_functionacyl-CoA dehydrogenase activity

Inferred from direct assay PubMed 9459013. Source: RGD

butyryl-CoA dehydrogenase activity

Inferred from direct assay PubMed 3968063PubMed 8952487. Source: RGD

fatty-acyl-CoA binding

Inferred from direct assay PubMed 3968063PubMed 8952487. Source: RGD

flavin adenine dinucleotide binding

Inferred from direct assay PubMed 3968063PubMed 8952487. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2424Mitochondrion
Chain25 – 412388Short-chain specific acyl-CoA dehydrogenase, mitochondrial
PRO_0000000501

Regions

Nucleotide binding152 – 16110FAD
Nucleotide binding185 – 1873FAD
Nucleotide binding365 – 3695FAD
Nucleotide binding394 – 3963FAD
Region269 – 2724Substrate binding

Sites

Active site3921Proton acceptor
Binding site1611Substrate; via carbonyl oxygen
Binding site2971FAD
Binding site3081FAD By similarity
Binding site3931Substrate; via amide nitrogen

Amino acid modifications

Modified residue511N6-acetyllysine; alternate By similarity
Modified residue511N6-succinyllysine; alternate By similarity
Modified residue721N6-acetyllysine By similarity
Modified residue1291N6-acetyllysine; alternate By similarity
Modified residue1291N6-succinyllysine; alternate By similarity
Modified residue2081N6-acetyllysine By similarity
Modified residue2621N6-acetyllysine; alternate By similarity
Modified residue2621N6-succinyllysine; alternate By similarity
Modified residue2921N6-acetyllysine By similarity
Modified residue3061N6-acetyllysine; alternate By similarity
Modified residue3061N6-succinyllysine; alternate By similarity

Secondary structure

............................................................ 412
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15651 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 3E4A052FC99B8E14

FASTA41244,765
        10         20         30         40         50         60 
MAAALLARAG GSLGRALRAR DWRRLHTVYQ SVELPETHQM LRQTCRDFAE KELVPIAAQL 

        70         80         90        100        110        120 
DKEHLFPTSQ VKKMGELGLL AMDVPEELSG AGLDYLAYSI ALEEISRGCA STGVIMSVNN 

       130        140        150        160        170        180 
SLYLGPILKF GSSQQKQQWI TPFTNGDKIG CFALSEPGNG SDAGAASTTA REEGDSWVLN 

       190        200        210        220        230        240 
GTKAWITNSW EASATVVFAS TDRSRQNKGI SAFLVPMPTP GLTLGKKEDK LGIRASSTAN 

       250        260        270        280        290        300 
LIFEDCRIPK ENLLGEPGMG FKIAMQTLDM GRIGIASQAL GIAQASLDCA VKYAENRHAF 

       310        320        330        340        350        360 
GAPLTKLQNI QFKLADMALA LESARLLTWR AAMLKDNKKP FTKESAMAKL AASEAATAIS 

       370        380        390        400        410 
HQAIQILGGM GYVTEMPAER YYRDARITEI YEGTSEIQRL VIAGHLLRSY RS 

« Hide

References

[1]"Molecular cloning and nucleotide sequence of cDNAs encoding the precursors of rat long chain acyl-coenzyme A, short chain acyl-coenzyme A, and isovaleryl-coenzyme A dehydrogenases. Sequence homology of four enzymes of the acyl-CoA dehydrogenase family."
Matsubara Y., Indo Y., Naito E., Ozasa H., Glassberg R., Vockley J., Ikeda Y., Kraus J., Tanaka K.
J. Biol. Chem. 264:16321-16331(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"Crystal structure of rat short chain acyl-CoA dehydrogenase complexed with acetoacetyl-CoA: comparison with other acyl-CoA dehydrogenases."
Battaile K.P., Molin-Case J., Paschke R., Wang M., Bennett D., Vockley J., Kim J.-J.P.
J. Biol. Chem. 277:12200-12207(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 25-412 IN COMPLEX WITH ACETOACETYL-COA AND FAD, HOMOTETRAMERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05030 mRNA. Translation: AAA40669.1. Different initiation.
PIRB34252.
RefSeqNP_071957.1. NM_022512.2.
UniGeneRn.1167.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JQIX-ray2.25A/B25-412[»]
ProteinModelPortalP15651.
SMRP15651. Positions 28-411.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP15651. 1 interaction.
STRING10116.ENSRNOP00000001556.

Chemistry

ChEMBLCHEMBL2176825.

Proteomic databases

PaxDbP15651.
PRIDEP15651.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID64304.
KEGGrno:64304.
UCSCRGD:620514. rat.

Organism-specific databases

CTD35.
RGD620514. Acads.

Phylogenomic databases

eggNOGCOG1960.
HOVERGENHBG000224.
InParanoidP15651.
KOK00248.

Enzyme and pathway databases

SABIO-RKP15651.
UniPathwayUPA00660.

Gene expression databases

GenevestigatorP15651.

Family and domain databases

Gene3D1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProIPR006089. Acyl-CoA_DH_CS.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
PfamPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP15651.
NextBio612942.
PROP15651.

Entry information

Entry nameACADS_RAT
AccessionPrimary (citable) accession number: P15651
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways